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P48591

- RIR1_DROME

UniProt

P48591 - RIR1_DROME

Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

RnrL

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      Previous versions | rss
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    Functioni

    Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.

    Catalytic activityi

    2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.

    Enzyme regulationi

    Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the M1 subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei16 – 161Allosteric activatorBy similarity
    Binding sitei64 – 641Allosteric activatorBy similarity
    Binding sitei99 – 991Allosteric activatorBy similarity
    Binding sitei213 – 2131SubstrateBy similarity
    Sitei229 – 2291Important for hydrogen atom transferBy similarity
    Sitei237 – 2371Allosteric effector binding, determines substrate specificityBy similarity
    Binding sitei258 – 2581Substrate; via amide nitrogenBy similarity
    Sitei267 – 2671Allosteric effector binding, determines substrate specificityBy similarity
    Active sitei438 – 4381Proton acceptorBy similarity
    Active sitei440 – 4401Cysteine radical intermediateBy similarity
    Active sitei442 – 4421Proton acceptorBy similarity
    Sitei455 – 4551Important for hydrogen atom transferBy similarity
    Sitei748 – 7481Important for electron transferBy similarity
    Sitei749 – 7491Important for electron transferBy similarity
    Sitei807 – 8071Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei810 – 8101Interacts with thioredoxin/glutaredoxinBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: FlyBase
    2. deoxyribonucleotide biosynthetic process Source: UniProtKB
    3. DNA replication Source: UniProtKB-UniPathway
    4. tissue regeneration Source: FlyBase

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00326.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonucleoside-diphosphate reductase large subunit (EC:1.17.4.1)
    Alternative name(s):
    Ribonucleoside-diphosphate reductase subunit M1
    Ribonucleotide reductase large subunit
    Gene namesi
    Name:RnrL
    ORF Names:CG5371
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0011703. RnrL.

    Subcellular locationi

    GO - Cellular componenti

    1. ribonucleoside-diphosphate reductase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 812812Ribonucleoside-diphosphate reductase large subunitPRO_0000187193Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi229 ↔ 455Redox-activeBy similarity
    Modified residuei778 – 7781Phosphothreonine1 Publication
    Modified residuei782 – 7821Phosphoserine1 Publication
    Modified residuei786 – 7861Phosphotyrosine1 Publication

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    PaxDbiP48591.

    Expressioni

    Gene expression databases

    BgeeiP48591.

    Interactioni

    Subunit structurei

    Heterodimer of a large and a small subunit.

    Protein-protein interaction databases

    BioGridi60477. 3 interactions.
    DIPiDIP-19582N.
    MINTiMINT-829510.

    Structurei

    3D structure databases

    ProteinModelPortaliP48591.
    SMRiP48591. Positions 26-753.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 10392ATP-conePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni22 – 287Allosteric activator bindingBy similarity
    Regioni228 – 2292Substrate bindingBy similarity
    Regioni296 – 2994Allosteric effector binding, determines substrate specificityBy similarity
    Regioni438 – 4425Substrate bindingBy similarity
    Regioni614 – 6185Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 1 ATP-cone domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0209.
    GeneTreeiENSGT00390000001372.
    InParanoidiP48591.
    KOiK10807.
    OMAiEACLMCQ.
    OrthoDBiEOG7BGHK2.
    PhylomeDBiP48591.

    Family and domain databases

    InterProiIPR005144. ATP-cone.
    IPR013346. NrdE_NrdA.
    IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    IPR008926. RNR_R1-su_N.
    [Graphical view]
    PfamiPF03477. ATP-cone. 1 hit.
    PF02867. Ribonuc_red_lgC. 1 hit.
    PF00317. Ribonuc_red_lgN. 1 hit.
    [Graphical view]
    PRINTSiPR01183. RIBORDTASEM1.
    SUPFAMiSSF48168. SSF48168. 1 hit.
    TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
    PROSITEiPS51161. ATP_CONE. 1 hit.
    PS00089. RIBORED_LARGE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P48591-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLKNKSMKTS KLYVIKRDGR QEEVHFDKIT SRIQKLCYNL NMDFVDPVTI    50
    TLQVINGLYC GVTTQELDNL AAEIAAGLTC NHPDYAILAA RIAVSNLHKE 100
    TKKAFSDVFE DLYNHVNKET NQKVPLVSEF HYNVVKKNAT RLNSSIIYDR 150
    DFGYNYFGFK TLERSYLLKR NGKIAERPQH MLMRVAIGIH GEDIDAAVET 200
    YNLLSERYFT HASPTLFAAA TNRPQLSSCF LLTMTADSIE GIFKSVEQCA 250
    MISKSAGGIG LNVHCIRAKG TSICGTNGTS NGLVPMLRVF NNVARYVDQG 300
    GGKRPGAFAI YLEPWHSDVF EFLELKKNTG KEENRARDLF YALWIPDLFM 350
    KRVEANGDWS LMCPHKCPGL HDVWGDEFEK LYEKYEQEGR ANRTVKAQSL 400
    WFAIIEAQVE TGNPYMLFKD ACNRKSNQQN VGTIKCSNLC TEIVEYSAPD 450
    EIAVCNLASI ALNMFVTPEK TYDFKKLKEV TKIVTKNLNK IIDINYYPLP 500
    EARKSNLRHR PVGIGIQGFA DALILMRFPY ESEEAGLLNQ QIFETIYYGA 550
    LEASCELAQT EGPYETYEGS PVSKGILQYD MWDKVPTNLW DWQKLKESIR 600
    MHGVRNSLLV APMPTASTAQ IMGNNESFEP YTTNIYTRRV LSGEFQVVNH 650
    HLLRDLTELD LWDDDMKNQI ISSRGSIQNI ETIPPKVRDL YKTVWEISVK 700
    STIKMAADRG AFIDQSQSFN IHVAEPNYGK LTSIHFYSWK AGLKTGMYYL 750
    RTKPAANAIQ FTVNKKQGAV SMNGQNGTAE GSPQKYEEDR ERKMADMVCS 800
    LENKDACMSC GS 812
    Length:812
    Mass (Da):91,978
    Last modified:December 1, 2000 - v2
    Checksum:i6E4FC608AC04A5FD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014134 Genomic DNA. Translation: AAF52913.2.
    AF132143 mRNA. Translation: AAD33590.1.
    AY119149 mRNA. Translation: AAM51009.1.
    U09369 Genomic DNA. Translation: AAA56995.1.
    RefSeqiNP_477027.1. NM_057679.5.
    UniGeneiDm.3216.

    Genome annotation databases

    EnsemblMetazoaiFBtr0080059; FBpp0079648; FBgn0011703.
    GeneIDi34392.
    KEGGidme:Dmel_CG5371.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014134 Genomic DNA. Translation: AAF52913.2 .
    AF132143 mRNA. Translation: AAD33590.1 .
    AY119149 mRNA. Translation: AAM51009.1 .
    U09369 Genomic DNA. Translation: AAA56995.1 .
    RefSeqi NP_477027.1. NM_057679.5.
    UniGenei Dm.3216.

    3D structure databases

    ProteinModelPortali P48591.
    SMRi P48591. Positions 26-753.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 60477. 3 interactions.
    DIPi DIP-19582N.
    MINTi MINT-829510.

    Proteomic databases

    PaxDbi P48591.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0080059 ; FBpp0079648 ; FBgn0011703 .
    GeneIDi 34392.
    KEGGi dme:Dmel_CG5371.

    Organism-specific databases

    CTDi 34392.
    FlyBasei FBgn0011703. RnrL.

    Phylogenomic databases

    eggNOGi COG0209.
    GeneTreei ENSGT00390000001372.
    InParanoidi P48591.
    KOi K10807.
    OMAi EACLMCQ.
    OrthoDBi EOG7BGHK2.
    PhylomeDBi P48591.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .

    Miscellaneous databases

    GenomeRNAii 34392.
    NextBioi 788275.
    PROi P48591.

    Gene expression databases

    Bgeei P48591.

    Family and domain databases

    InterProi IPR005144. ATP-cone.
    IPR013346. NrdE_NrdA.
    IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    IPR008926. RNR_R1-su_N.
    [Graphical view ]
    Pfami PF03477. ATP-cone. 1 hit.
    PF02867. Ribonuc_red_lgC. 1 hit.
    PF00317. Ribonuc_red_lgN. 1 hit.
    [Graphical view ]
    PRINTSi PR01183. RIBORDTASEM1.
    SUPFAMi SSF48168. SSF48168. 1 hit.
    TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
    PROSITEi PS51161. ATP_CONE. 1 hit.
    PS00089. RIBORED_LARGE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    2. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    4. "Developmental control of a G1-S transcriptional program in Drosophila."
      Duronio R.J., O'Farrell P.H.
      Development 120:1503-1515(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-343.
      Strain: Oregon-R.
    5. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-778; SER-782 AND TYR-786, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiRIR1_DROME
    AccessioniPrimary (citable) accession number: P48591
    Secondary accession number(s): Q9UB08, Q9VKZ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 118 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3